Reviewed, UniProtKB/Swiss-Prot Q1Q8J9 (FADB_PSYCK)

Names and origin

Protein names

Recommended name:
    Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
    1- Recommended name:
            Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
              EC=4.2.1.17
              EC=5.3.3.8
              EC=5.1.2.3
    2- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35

Gene names

Name:	fadB
Ordered Locus Names:	Pcryo_2227

Organism

Psychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]

Taxonomic identifier

335284 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Psychrobacter

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the formation of an hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities By similarity.
Catalytic activity	(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP MF_01621 (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP MF_01621 (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP MF_01621 (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP MF_01621
Pathway	Lipid metabolism; fatty acid beta-oxidation. HAMAP MF_01621
Subunit structure	Heterotetramer of two alpha chains (fadB) and two beta chains (fadA) By similarity.
Sequence similarities	In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid degradation Lipid metabolism
Ligand	NAD
Molecular function	Isomerase Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid catabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fatty acid beta-oxidation multienzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	3-hydroxyacyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 3-hydroxybutyryl-CoA epimerase activity Inferred from electronic annotation. Source: HAMAP coenzyme binding Inferred from electronic annotation. Source: InterPro dodecenoyl-CoA delta-isomerase activity Inferred from electronic annotation. Source: HAMAP enoyl-CoA hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 719	719	Fatty acid oxidation complex subunit alpha HAMAP MF_01621		PRO_0000255844
Regions
	Region	1 – 190	190	Enoyl-CoA hydratase/isomerase By similarity
	Region	313 – 719	407	3-hydroxyacyl-CoA dehydrogenase By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1Q8J9-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 0A15859CAFCD9966	FASTA	719	78,378
	10 20 30 40 50 60 MVYQGNRITV TMLEDGIANM QYNAENESVN KFDTETNKQF AEVVNALEKA DDIKGLIVTS 70 80 90 100 110 120 SKGVFIAGAD ITEFVASFKQ SEEEIKDWVI NINDAFNRFE DLPFPKVAAI NGAALGGGCE 130 140 150 160 170 180 MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG GTVRSTRVIG IDNALELIAT GTPKKALDAL 190 200 210 220 230 240 KLGLVDATVA ADDLQDAAID LVKKCISDEL DWQAKREEKL VPVKLNQLEQ AMAFNSAKGM 250 260 270 280 290 300 IFAKANPKQY PAPALAIAAI EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL 310 320 330 340 350 360 VKKLAKQHSK KAHDINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ LDLGMGEASK 370 380 390 400 410 420 LLGKMVDRGK ITPAKMGETL SRIRPTLNYG DFAETDIVIE AVVENPNVKR AVLKEVEGLV 430 440 450 460 470 480 KDDCILASNT STISITFLAE ALERPENFVG MHFFNPVNRM PLVEVIRGEK SSEEAISTTV 490 500 510 520 530 540 ALATKMGKVP VVVNDCPGFL VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY 550 560 570 580 590 600 LIDVVGLDTG VHGAEVMAEG FPDRMKPDYK GAIEHLYENK RLGQKNGVGF YKYEMDKRGK 610 620 630 640 650 660 PKKVADEATY ELLKTTTDSD KQTFEDQAII DRTMLAFCNE TVRCLEDNIV STPSEADMAM 670 680 690 700 710 IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAYLGKAYE APQKIRDMAA AGETFYATA

References

[1]

"Complete sequence of chromosome of Psychrobacter cryohalolentis K5." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000323 Genomic DNA. Translation: ABE76004.1.
RefSeq	YP_581488.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4033840.
GenomeReviews	Gene locus Pcryo_2227 in contig CP000323_GR.
KEGG	pcr:Pcryo_2227.
NMPDR	fig|335284.3.peg.2207.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1Q8J9.
OMA	Q1Q8J9. ANNGSYY.
Enzyme and pathway databases
BioCyc	PCRY335284:PCRYO_2227-MON.
Family and domain databases
HAMAP	MF_01621. [Tree]
InterPro	IPR006180. 3-OHacyl-CoA_DH_CS. IPR006176. 3-OHacyl-CoA_DH_NAD-bd. IPR006108. 3HC_DH_C. IPR001753. Crotonase_core. IPR013328. DH_multihelical. IPR018376. Enoyl-CoA_hyd/isom_CS. IPR012799. FadB. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
Pfam	PF00725. 3HCDH. 1 hit. PF02737. 3HCDH_N. 1 hit. PF00378. ECH. 1 hit. [Graphical view]
TIGRFAMs	TIGR02437. FadB. 1 hit.
PROSITE	PS00067. 3HCDH. 1 hit. PS00166. ENOYL_COA_HYDRATASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FADB_PSYCK

Accession

Primary (citable) accession number: Q1Q8J9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 16, 2006
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)